ID H9UE23_FERPD Unreviewed; 312 AA.
AC H9UE23;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Type-2 restriction enzyme {ECO:0000256|PIRNR:PIRNR016080};
DE EC=3.1.21.4 {ECO:0000256|PIRNR:PIRNR016080};
GN OrderedLocusNames=Ferpe_1710 {ECO:0000313|EMBL:AFG35766.1};
OS Fervidobacterium pennivorans (strain DSM 9078 / Ven5).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=771875 {ECO:0000313|EMBL:AFG35766.1, ECO:0000313|Proteomes:UP000007384};
RN [1] {ECO:0000313|Proteomes:UP000007384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9078 / Ven5 {ECO:0000313|Proteomes:UP000007384};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Noll K.M., Woyke T.;
RT "Complete sequence of Fervidobacterium pennivorans DSM 9078.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC stranded unmethylated sequence 5'-GATC-3'.
CC {ECO:0000256|PIRNR:PIRNR016080}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC Evidence={ECO:0000256|PIRNR:PIRNR016080};
CC -!- SIMILARITY: Belongs to the DpnII type II restriction endonuclease
CC family. {ECO:0000256|PIRNR:PIRNR016080}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003260; AFG35766.1; -; Genomic_DNA.
DR RefSeq; WP_014452199.1; NC_017095.1.
DR AlphaFoldDB; H9UE23; -.
DR STRING; 771875.Ferpe_1710; -.
DR REBASE; 46323; Fpe9078ORF1709P.
DR KEGG; fpe:Ferpe_1710; -.
DR PATRIC; fig|771875.3.peg.1729; -.
DR eggNOG; ENOG502Z7V5; Bacteria.
DR HOGENOM; CLU_089327_0_0_0; -.
DR OMA; GLEQIFC; -.
DR OrthoDB; 9771872at2; -.
DR Proteomes; UP000007384; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-UniRule.
DR InterPro; IPR021191; Restrct_endonuc_II_DpnII.
DR InterPro; IPR007637; Restrct_endonuc_II_DpnII-like.
DR Pfam; PF04556; DpnII; 1.
DR PIRSF; PIRSF016080; Restrict_endonuc_II_DpmII; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|PIRNR:PIRNR016080, ECO:0000313|EMBL:AFG35766.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR016080};
KW Nuclease {ECO:0000256|PIRNR:PIRNR016080};
KW Restriction system {ECO:0000256|PIRNR:PIRNR016080}.
FT DOMAIN 24..306
FT /note="Restriction endonuclease type II DpnII-like"
FT /evidence="ECO:0000259|Pfam:PF04556"
SQ SEQUENCE 312 AA; 36468 MW; 96050DBD9494F0CE CRC64;
MDSTYLHILQ KKGLKVSNTE DLMKIFLDTL LETNKTYDFF VDWKKVRTFV EKNKVEINIL
NSLLHSEDFD NELRRILRKY PEVLKVVPLL LAIRDNSVSI ISEFDLEKTN VIKLDFTERN
LREEEIEIFV DFFKKTGLKD FFLNVADKSL LDYILGVEVG MDTNARKNRS GKVLENFLKP
IIEKIANDLK CTFLTQEKFS TLEKYSININ KLKDRKADFI LLKPRGDGSY GVVNIEVNFY
NVSGSKPQEI IDSYIERQKE LKEYGYEFLL ITDGPAWKEQ KSQLTKALEN LDFVLNTYLV
RLGILEEVIC MI
//